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Volumn 5, Issue 7, 2010, Pages 667-680

Proteomic and mass spectroscopic quantitation of protein s-nitrosation differentiates NO-donors

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GLUTATHIONE TRANSFERASE P1; GLUTATHIONE TRANSFERASE P1 1; HELICASE; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; NITRIC OXIDE DONOR; OXIDIZING AGENT; OXYGEN; PROTEIN S; S NITROSOTHIOL; THIOL; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG;

EID: 77955042985     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb100054m     Document Type: Article
Times cited : (40)

References (69)
  • 2
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamler J.S., Singel, D.J., and Loscalzo J. (1992) Biochemistry of nitric oxide and its redox-activated forms, Science 258 1898-1902.
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 3
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches
    • Paulsen, C. E., and Carroll, K. S. (2010) Orchestrating redox signaling networks through regulatory cysteine switches, ACS Chem. Biol. 5 47-62.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 47-62
    • Paulsen, C.E.1    Carroll, K.S.2
  • 4
    • 0035849714 scopus 로고    scopus 로고
    • S-nitrosylation is emerging as a specific and fundamental posttranslational protein modification: Head-to-head comparison with O-phosphorylation
    • re1
    • Lane, P., Hao, G., and Gross, S. S. (2001) S-Nitrosylation is emerging as a specific and fundamental posttranslational protein modification: head-to-head comparison with O-phosphorylation, Sci. STKE (86), re1.
    • (2001) Sci. STKE , Issue.86
    • Lane, P.1    Hao, G.2    Gross, S.S.3
  • 6
    • 77949370996 scopus 로고    scopus 로고
    • S-nitrosylation in cardiovascular signaling
    • Lima, B., Forrester, M. T., Hess, D. T., and Stamler, J. S. (2010) S-Nitrosylation in cardiovascular signaling, Circ. Res. 106, 633-646.
    • (2010) Circ. Res. , vol.106 , pp. 633-646
    • Lima, B.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 7
    • 0030662226 scopus 로고    scopus 로고
    • Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms
    • Kim, Y. M., Talanian, R. V., and Billiar, T. R. (1997) Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms, J. Biol. Chem. 272, 31138-31148.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31138-31148
    • Kim, Y.M.1    Talanian, R.V.2    Billiar, T.R.3
  • 8
    • 15444379675 scopus 로고    scopus 로고
    • S-nitrosation and regulation of inducible nitric oxide synthase
    • Mitchell, D. A., Erwin, P. A., Michel, T., and Marletta, M. A. (2005) S-Nitrosation and regulation of inducible nitric oxide synthase, Biochemistry 44, 4636-4647.
    • (2005) Biochemistry , vol.44 , pp. 4636-4647
    • Mitchell, D.A.1    Erwin, P.A.2    Michel, T.3    Marletta, M.A.4
  • 9
    • 0028106016 scopus 로고
    • Glutathione-associated enzymes in anticancer drug resistance
    • Tew, K. D. (1994) Glutathione-associated enzymes in anticancer drug resistance, Cancer Res. 54,4313-4320.
    • (1994) Cancer Res. , vol.54 , pp. 4313-4320
    • Tew, K.D.1
  • 13
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • Jaffrey, S. R., and Snyder, S. H. (2001) The biotin switch method for the detection of S-nitrosylated proteins, Sci. STKE (86), p 11.
    • (2001) Sci. STKE , Issue.86 , pp. 11
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 15
    • 17644386593 scopus 로고    scopus 로고
    • Inhibition of protein-tyrosine phosphatases by mild oxidative stresses is dependent on S-nitrosylation
    • Barrett, D. M., Black, S. M., Todor, H., Schmidt-Ullrich, R. K., Dawson, K. S., and Mikkelsen, R. B. (2005) Inhibition of protein-tyrosine phosphatases by mild oxidative stresses is dependent on S-nitrosylation, J. Biol. Chem. 280,14453-14461.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14453-14461
    • Barrett, D.M.1    Black, S.M.2    Todor, H.3    Schmidt-Ullrich, R.K.4    Dawson, K.S.5    Mikkelsen, R.B.6
  • 17
    • 53249088371 scopus 로고    scopus 로고
    • Nitroglycerin-induced S-nitrosylation and desensitization of soluble guanylyl cyclase contribute to nitrate tolerance
    • Sayed, N., Kim, D. D., Fioramonti, X., Iwahashi, T., Duran, W. N., and Beuve, A. (2008) Nitroglycerin-induced S-nitrosylation and desensitization of soluble guanylyl cyclase contribute to nitrate tolerance, Circ. Res. 103,606-614.
    • (2008) Circ. Res. , vol.103 , pp. 606-614
    • Sayed, N.1    Kim, D.D.2    Fioramonti, X.3    Iwahashi, T.4    Duran, W.N.5    Beuve, A.6
  • 19
    • 67349161335 scopus 로고    scopus 로고
    • Activation and inhibition of soluble guanylyl cyclase by snitrosocysteine: Involvement of amino acid transport system L
    • Riego, J. A., Broniowska, K. A., Kettenhofen, N. J., and Hogg, N. (2009) Activation and inhibition of soluble guanylyl cyclase by Snitrosocysteine: involvement of amino acid transport system L, Free Radicol Biol. Med. 47, 269-274.
    • (2009) Free Radicol Biol. Med. , vol.47 , pp. 269-274
    • Riego, J.A.1    Broniowska, K.A.2    Kettenhofen, N.J.3    Hogg, N.4
  • 21
    • 38149123809 scopus 로고    scopus 로고
    • Organic nitrates and nitrites as stores of NO
    • (van Fassen, E., and Vanin, A., Eds.), ElsevierScience, Amsterdam
    • Thatcher, G. R.J. (2007) Organic nitrates and nitrites as stores of NO, in Radicals for Life: The Various Forms of Nitric Oxide (van Fassen, E., and Vanin, A., Eds.), Elsevier Science, Amsterdam.
    • (2007) Radicals for Life: The Various Forms of Nitric Oxide
    • Thatcher, G.R.J.1
  • 22
    • 23844503998 scopus 로고    scopus 로고
    • An introduction to NO-related therapeutic agents
    • Thatcher, G. R. J. (2005) An introduction to NO-related therapeutic agents, Curr. Top. Med. Chem. 5, 597-601.
    • (2005) Curr. Top. Med. Chem. , vol.5 , pp. 597-601
    • Thatcher, G.R.J.1
  • 23
    • 4644231576 scopus 로고    scopus 로고
    • Nitrates and NO release: Contemporary aspects in biological and medicinal chemistry
    • Thatcher, G. R. J., Nicolescu, A. C., Bennett, B. M., and Toader, V. (2004) Nitrates and NO release: Contemporary aspects in biological and medicinal chemistry, Free Radical Biol. Med. 37,1122-1143.
    • (2004) Free Radical Biol. Med. , vol.37 , pp. 1122-1143
    • Thatcher, G.R.J.1    Nicolescu, A.C.2    Bennett, B.M.3    Toader, V.4
  • 26
    • 0014105888 scopus 로고
    • Enzyme-catalysed conjugations of glutathione with unsaturated compounds
    • Boyland, E., and Chasseaud, L. F. (1967) Enzyme-catalysed conjugations of glutathione with unsaturated compounds, Biochem. J. 104, 95-102.
    • (1967) Biochem. J. , vol.104 , pp. 95-102
    • Boyland, E.1    Chasseaud, L.F.2
  • 27
    • 0035901523 scopus 로고    scopus 로고
    • Structural and functional consequences of inactivation of human glutathione S-transferase P1-1 mediated by the catechol metabolite of equine estrogens, 4-hydroxyequilenin
    • Chang, M., Shin, Y. G., van Breemen, R. B., Blond, S. Y., and Bolton, J. L. (2001) Structural and functional consequences of inactivation of human glutathione S-transferase P1-1 mediated by the catechol metabolite of equine estrogens, 4-hydroxyequilenin, Biochemistry 40, 4811-4820.
    • (2001) Biochemistry , vol.40 , pp. 4811-4820
    • Chang, M.1    Shin, Y.G.2    Van Breemen, R.B.3    Blond, S.Y.4    Bolton, J.L.5
  • 28
    • 49049114502 scopus 로고    scopus 로고
    • Problematic detoxification of estrogen quinones by NAD(P)H-dependent quinone oxidoreductase and glutathione-S-transferase
    • Chandrasena, R. E., Edirisinghe, P. D., Bolton, J. L., and Thatcher, G. R. (2008) Problematic detoxification of estrogen quinones by NAD(P)H-dependent quinone oxidoreductase and glutathione-S-transferase, Chem. Res. Toxicol. 21,1324-1329.
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 1324-1329
    • Chandrasena, R.E.1    Edirisinghe, P.D.2    Bolton, J.L.3    Thatcher, G.R.4
  • 29
    • 25444462779 scopus 로고    scopus 로고
    • Analysis of protein covalent modification byxenobiotics using a covert oxidatively activated tag: Raloxifene proof-of-principle study
    • Liu, J., Li, Q., Yang, X., van Breemen, R. B., Bolton, J. L., and Thatcher, G. R. (2005) Analysis of protein covalent modification byxenobiotics using a covert oxidatively activated tag: raloxifene proof-of-principle study, Chem. Res. Toxicol. 18,1485-1496.
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 1485-1496
    • Liu, J.1    Li, Q.2    Yang, X.3    Van Breemen, R.B.4    Bolton, J.L.5    Thatcher, G.R.6
  • 31
    • 0142242187 scopus 로고    scopus 로고
    • The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily: Suggestion for an evolutionary pressure in the direction of the storage of nitric oxide
    • De Maria, F., Pedersen, J. Z., Caccuri, A. M., Antonini, G., Turella, P., Stella, L., Lo Bello, M., Federici, G., and Ricci, G. (2003) The specific interaction of dinitrosyl-diglutathionyl-iron complex, a natural NO carrier, with the glutathione transferase superfamily: suggestion for an evolutionary pressure in the direction of the storage of nitric oxide, J. Biol. Chem. 278, 42283-42293.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42283-42293
    • De Maria, F.1    Pedersen, J.Z.2    Caccuri, A.M.3    Antonini, G.4    Turella, P.5    Stella, L.6    Lo Bello, M.7    Federici, G.8    Ricci, G.9
  • 32
    • 37049084926 scopus 로고
    • Nitrosation by alkyl nitrites. Part 3. Reactions with cysteine in water in the pH range6-13
    • Patel, H. M.S., and Williams, D. L. H. (1989) Nitrosation by alkyl nitrites. Part 3. Reactions with cysteine in water in the pH range 6-13, J. Chem. Soc., Perkin Trans. 2 339-341.
    • (1989) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 339-341
    • Patel, H.M.S.1    Williams, D.L.H.2
  • 35
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg, N. (2002) The biochemistry and physiology of S-nitrosothiols, Annu. Rev. Pharmacol. Toxicol. 42, 585-600.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 585-600
    • Hogg, N.1
  • 36
    • 0028987969 scopus 로고
    • NO+, NO, and NO-donation by S-nitrosothiols: Implications for regulation of physiological functions byS-nitrosylation and acceleration of disulfide formation
    • Arnelle, D. R., and Stamler, J.S. (1995) NO+, NO, and NO- donation by S-nitrosothiols: implications for regulation of physiological functions byS-nitrosylation and acceleration of disulfide formation, Arch. Biochem. Biophys. 318, 279-285.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 279-285
    • Arnelle, D.R.1    Stamler, J.S.2
  • 37
    • 0032382795 scopus 로고    scopus 로고
    • NO problem for nitroglycerin: Organic nitrate chemistry and therapy
    • Thatcher, G. R. J., and Weldon, H. (1998) NO problem for nitroglycerin: organic nitrate chemistry and therapy, Chem. Soc. Rev. 27, 331-337. (Pubitemid 128653115)
    • (1998) Chemical Society Reviews , vol.27 , Issue.5 , pp. 331-337
    • Thatcher, G.R.J.1    Weldon, H.2
  • 38
    • 40949098241 scopus 로고    scopus 로고
    • Copper dependence of the biotin switch assay: Modified assay for measuring cellular and blood nitrosated proteins
    • Wang, X., Kettenhofen, N. J., Shiva, S., Hogg, N., and Gladwin, M. T. (2008) Copper dependence of the biotin switch assay: modified assay for measuring cellular and blood nitrosated proteins, Free Radical Biol. Med. 44,1362-1372.
    • (2008) Free Radical Biol. Med. , vol.44 , pp. 1362-1372
    • Wang, X.1    Kettenhofen, N.J.2    Shiva, S.3    Hogg, N.4    Gladwin, M.T.5
  • 40
    • 1342289357 scopus 로고    scopus 로고
    • Organic nitrites and NO: Inhibition of lipid peroxidation and radical reactions
    • Nicolescu, A. C., Reynolds, J. N., Barclay, L R., and Thatcher, G. R. J. (2004) Organic nitrites and NO: inhibition of lipid peroxidation and radical reactions, Chem. Res. Toxicol. 17,185-196.
    • (2004) Chem. Res. Toxicol. , vol.17 , pp. 185-196
    • Nicolescu, A.C.1    Reynolds, J.N.2    Barclay, L.R.3    Thatcher, G.R.J.4
  • 41
    • 37049084926 scopus 로고
    • Nitrosation by alkyl nitrites. Part 3. Reactions with cysteine in water in the pH range 6-13
    • Patel, H. M. S., and Williams, D. L H. (1989) Nitrosation by alkyl nitrites. Part 3. Reactions with cysteine in water in the pH range 6-13, J. Chem. Soc., Perkin Trans. 2 339-341.
    • (1989) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 339-341
    • Patel, H.M.S.1    Williams, D.L.H.2
  • 42
    • 57449110511 scopus 로고    scopus 로고
    • Kinetic analysis of intracellular concentrations of reactive nitrogen species
    • Lim, C. H., Dedon, P. C., and Deen, W. M. (2008) Kinetic analysis of intracellular concentrations of reactive nitrogen species, Chem. Res. Toxicol. 21, 2134-2147.
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 2134-2147
    • Lim, C.H.1    Dedon, P.C.2    Deen, W.M.3
  • 44
    • 33749005136 scopus 로고    scopus 로고
    • Nitroxidative, nitrosative, and nitrative stress: Kinetic predictions of reactive nitrogen species chemistry under biological conditions
    • Lancaster, J. R., Jr. (2006) Nitroxidative, nitrosative, and nitrative stress: kinetic predictions of reactive nitrogen species chemistry under biological conditions, Chem Res. Toxicol. 19 1160-1174.
    • (2006) Chem Res. Toxicol. , vol.19 , pp. 1160-1174
    • Lancaster Jr., J.R.1
  • 45
    • 74049084627 scopus 로고    scopus 로고
    • Reaction between nitric oxide, glutathione, and oxygen in the presence and absence of protein: How are S-nitrosothiols formed
    • Keszler, A., Zhang, Y., and Hogg, N. Reaction between nitric oxide, glutathione, and oxygen in the presence and absence of protein: How are S-nitrosothiols formed, Free Radical Biol. Med. 48 55-64.
    • Free Radical Biol. Med. , vol.48 , pp. 55-64
    • Keszler, A.1    Zhang, Y.2    Hogg, N.3
  • 46
  • 47
    • 0033168205 scopus 로고    scopus 로고
    • Critical role of sulfenic acid formation of thiols in the inactivation of glyceraldehyde-3-phosphate dehydrogenase by nitric oxide
    • Ishii, T., Sunami, O., Nakajima, H., Nishio, H., Takeuchi, T., and Hata, F. (1999) Critical role of sulfenic acid formation of thiols in the inactivation of glyceraldehyde-3-phosphate dehydrogenase by nitric oxide, Biochem. Pharmacol. 58,133-143.
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 133-143
    • Ishii, T.1    Sunami, O.2    Nakajima, H.3    Nishio, H.4    Takeuchi, T.5    Hata, F.6
  • 48
    • 77950887186 scopus 로고    scopus 로고
    • Activation of NRF2 by nitrosative agents and H2O2 involves KEAP1 disulfide formation
    • Fourquet, S., Guerois, R., Biard, D., and Toledano, M. B. (2010) Activation of NRF2 by nitrosative agents and H2O2 involves KEAP1 disulfide formation, J. Biol. Chem. 285, 8463-8471.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8463-8471
    • Fourquet, S.1    Guerois, R.2    Biard, D.3    Toledano, M.B.4
  • 49
    • 34250734460 scopus 로고    scopus 로고
    • Design and characterization of an active site selective caspase-3 transnitrosating agent
    • Mitchell, D. A., Morton, S. U., and Marletta, M. A. (2006) Design and characterization of an active site selective caspase-3 transnitrosating agent, ACS Chem. Biol. 1,659-665.
    • (2006) ACS Chem. Biol. , vol.1 , pp. 659-665
    • Mitchell, D.A.1    Morton, S.U.2    Marletta, M.A.3
  • 50
    • 63049105321 scopus 로고    scopus 로고
    • MassMatrix: A database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data
    • Xu, H., and Freitas, M. A. (2009) MassMatrix: a database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data, Proteomics 9,1548-1555.
    • (2009) Proteomics , vol.9 , pp. 1548-1555
    • Xu, H.1    Freitas, M.A.2
  • 51
    • 57649198018 scopus 로고    scopus 로고
    • Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability
    • Paige, J. S., Xu, G., Stancevic, B., and Jaffrey, S. R. (2008) Nitrosothiol reactivity profiling identifies S-nitrosylated proteins with unexpected stability, Chem. Biol. 15,1307-1316.
    • (2008) Chem. Biol. , vol.15 , pp. 1307-1316
    • Paige, J.S.1    Xu, G.2    Stancevic, B.3    Jaffrey, S.R.4
  • 53
    • 0033896832 scopus 로고    scopus 로고
    • Glutathione S-transferase p elicits protection against H2O2-induced cell death via coordinated regulation of stress kinases
    • Yin, Z., Ivanov, V. N., Habelhah, H., Tew, K., and Ronai, Z. (2000) Glutathione S-transferase p elicits protection against H2O2-induced cell death via coordinated regulation of stress kinases, Cancer Res. 60, 4053-4057.
    • (2000) Cancer Res. , vol.60 , pp. 4053-4057
    • Yin, Z.1    Ivanov, V.N.2    Habelhah, H.3    Tew, K.4    Ronai, Z.5
  • 54
    • 58649100268 scopus 로고    scopus 로고
    • Novel role for glutathione S-transferase pi. Regulator of protein S-glutathionylation following oxidative and nitrosative stress
    • Townsend, D. M., Manevich, Y., He, L., Hutchens, S., Pazoles, C.J., and Tew, K. D. (2009) Novel role for glutathione S-transferase pi. Regulator of protein S-Glutathionylation following oxidative and nitrosative stress, J. Biol. Chem. 284, 436-445.
    • (2009) J. Biol. Chem. , vol.284 , pp. 436-445
    • Townsend, D.M.1    Manevich, Y.2    He, L.3    Hutchens, S.4    Pazoles, C.J.5    Tew, K.D.6
  • 56
    • 30744437425 scopus 로고    scopus 로고
    • Direct evidence forthe formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes
    • Ralat, L. A., Manevich, Y., Fisher, A. B., and Colman, R. F. (2006) Direct evidence forthe formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes, Biochemistry 45, 360-372.
    • (2006) Biochemistry , vol.45 , pp. 360-372
    • Ralat, L.A.1    Manevich, Y.2    Fisher, A.B.3    Colman, R.F.4
  • 57
    • 32244445145 scopus 로고    scopus 로고
    • SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures
    • Hao, G., Derakhshan, B., Shi, L., Campagne, F., and Gross, S. S. (2006) SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures, Proc. Natl. Acad. Sci. U.S.A. 103,1012-1017.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 1012-1017
    • Hao, G.1    Derakhshan, B.2    Shi, L.3    Campagne, F.4    Gross, S.S.5
  • 58
    • 34548152584 scopus 로고    scopus 로고
    • A novel approach to identify proteins modified by nitric oxide: The HIS-TAG switch method
    • Camerini, S., Polci, M. L., Restuccia, U., Usuelli, V., Malgaroli, A., and Bachi, A. (2007) A novel approach to identify proteins modified by nitric oxide: the HIS-TAG switch method, J. Proteome Res. 6, 3224-3231.
    • (2007) J. Proteome Res. , vol.6 , pp. 3224-3231
    • Camerini, S.1    Polci, M.L.2    Restuccia, U.3    Usuelli, V.4    Malgaroli, A.5    Bachi, A.6
  • 59
    • 42649106845 scopus 로고    scopus 로고
    • Detergent-free biotin switch combined with liquid chromatography/tandem mass spectrometry in the analysis of S-nitrosylated proteins
    • Han, P., and Chen, C. (2008) Detergent-free biotin switch combined with liquid chromatography/tandem mass spectrometry in the analysis of S-nitrosylated proteins, Rapid Commun. Mass Spectrom. 22, 1137-1145.
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 1137-1145
    • Han, P.1    Chen, C.2
  • 60
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics, Mol. Cell. Proteomics 1, 376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 61
    • 58049200135 scopus 로고    scopus 로고
    • Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidationinduced permanent inactivation
    • Chen, Y. Y., Chu, H. M., Pan, K. T., Teng, C. H., Wang, D. L., Wang, A. H., Khoo, K. H., and Meng, T. C. (2008) Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidationinduced permanent inactivation, J. Biol. Chem. 283, 35265-35272.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35265-35272
    • Chen, Y.Y.1    Chu, H.M.2    Pan, K.T.3    Teng, C.H.4    Wang, D.L.5    Wang, A.H.6    Khoo, K.H.7    Meng, T.C.8
  • 62
    • 33847069643 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: An initial assessment
    • Butterfield, D. A., Gnjec, A., Poon, H. F., Castegna, A., Pierce, W. M., Klein, J. B., and Martins, R. N. (2006) Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: an initial assessment, J. Alzheimers Dis. 10, 391-397.
    • (2006) J. Alzheimers Dis. , vol.10 , pp. 391-397
    • Butterfield, D.A.1    Gnjec, A.2    Poon, H.F.3    Castegna, A.4    Pierce, W.M.5    Klein, J.B.6    Martins, R.N.7
  • 63
    • 1642301524 scopus 로고    scopus 로고
    • Proteomic analysis of brain proteins in the gracile axonal dystrophy (gad) mouse, a syndrome that emanates from dysfunctional ubiquitin carboxylterminal hydrolase L-1, reveals oxidation of key proteins
    • Castegna, A., Thongboonkerd, V., Klein, J., Lynn, B. C., Wang, Y. L., Osaka, H., Wada, K., and Butterfield, D. A. (2004) Proteomic analysis of brain proteins in the gracile axonal dystrophy (gad) mouse, a syndrome that emanates from dysfunctional ubiquitin carboxylterminal hydrolase L-1, reveals oxidation of key proteins, J. Neurochem. 88,1540-1546.
    • (2004) J. Neurochem. , vol.88 , pp. 1540-1546
    • Castegna, A.1    Thongboonkerd, V.2    Klein, J.3    Lynn, B.C.4    Wang, Y.L.5    Osaka, H.6    Wada, K.7    Butterfield, D.A.8
  • 64
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi, J., Levey, A. I., Weintraub, S. T., Rees, H. D., Gearing, M., Chin, L. S., and Li, L. (2004) Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases, J. Biol. Chem. 279, 13256-13264.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6    Li, L.7
  • 65
    • 28444433110 scopus 로고    scopus 로고
    • Roles of distinct cysteine residues in S-nitrosylation and dimerization of DJ-1
    • Ito, G., Ariga, H., Nakagawa, Y., and Iwatsubo, T. (2006) Roles of distinct cysteine residues in S-nitrosylation and dimerization of DJ-1, Biochem. Biophys. Res. Commun. 339,667-672.
    • (2006) Biochem. Biophys. Res. Commun. , vol.339 , pp. 667-672
    • Ito, G.1    Ariga, H.2    Nakagawa, Y.3    Iwatsubo, T.4
  • 66
    • 2542516981 scopus 로고    scopus 로고
    • The mechanism of transmembrane S-nitrosothiol transport
    • Zhang, Y., and Hogg, N. (2004) The mechanism of transmembrane S-nitrosothiol transport, Proc. Natl. Acad. Sci. U.S.A. 101, 7891-7896.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 7891-7896
    • Zhang, Y.1    Hogg, N.2
  • 67
    • 0035902511 scopus 로고    scopus 로고
    • Old yellow enzyme: Reduction of nitrate esters, glycerin trinitrate, and propylene 1,2-dinitrate
    • Meah, Y., Brown, B.J., Chakraborty, S., and Massey, V. (2001) Old yellow enzyme: reduction of nitrate esters, glycerin trinitrate, and propylene 1,2-dinitrate, Proc. Natl. Acad. Sci. U.S.A. 98, 8560-8565.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8560-8565
    • Meah, Y.1    Brown, B.J.2    Chakraborty, S.3    Massey, V.4


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